Structure-activity relationships of peptides derived from ACTH, β-LPH and MSH with regard to avoidance behavior in rats

Nispen, J. W. van; Greven, H. M.

doi:10.1016/0163-7258(82)90032-8

Cited by 39 publications

(8 citation statements)

References 175 publications

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“…Thus, a-MSH displaced at most 25% and a-IFN 15% of total bound radioactivity. The observed affinity of a-MSH for the ACTH binding sites is in agree ment with data showing that these two poly peptides possess unique structure-activity relationships for different biological recep tors [6,7], This similarity has been attrib uted to their (4-10)-heptapeptide sequence that was indicated as essential for their ste roidogenic, melanotropic, lipolytic and be havioral properties [8]. The similarity of these two polypeptides with interferons was proposed on the basis of the finding that antiserum against the MSH-ACTH (1-13)-sequence neutralized a-IFN activity [9], as well as on evidence for ACTH-like activity of interferons in melanogenesis and ste roidogenesis [10,11].…”

Section: Resultssupporting

confidence: 74%

Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

Simić-Krstić

Ševaljević²

1988

Pathobiology

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The binding of adrenocorticotropic hormone (ACTH) to B16/C3 murine melanoma cells was found to be specific and saturable. The binding capacity of the cells changed as a function of the age of the culture. Scatchard analysis revealed one class of high-affinity ACTH binding sites. The specificity of ACTH binding to the cells was tested by displacement experiments with human leukocyte interferon (α-IFN) and α-melanocyte stimulating hormone (α-MSH) as the competitors. Structure-activity relationship of ACTH, α-MSH and α-IFN was discussed.

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Section: Resultssupporting

confidence: 74%

Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

Simić-Krstić

Ševaljević²

1988

Pathobiology

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“…most important, without measurable hormonal ac tions in the periphery' of the body (e.g. at the adrenal cor tex) [Van Nispen and Greven, 1982]. The mode of action of ACTH and its fragments within the CNS and the path ways of such effects after peripheral administration are presently only scarcely known.…”

Section: Neuroendocri Nologymentioning

confidence: 99%

ACTH and Attention in Humans:A Review

Born¹,

Fehm²,

Voigt³

1986

Neuropsychobiology

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In addition to the hormonal action of corticotropin (ACTH) on the adrenal cortex, this peptide and fragments of it may function as chemical signals in CNS synapses. This report reviews studies on behavioral and psychophysiological effects of ACTH-related neuropeptides. Experiments will be emphasized which applied EEG techniques for the measurement of peptide-induced changes on aspects of information processing in man. It is proposed to conceptualize the pattern of actions of ACTH-related neuropeptides as a blocking of suppressive functions occurring, for example, during habituation or selective attention. Disinhibitory effects mediated by structures of the limbic system may be responsible for repeatedly observed improvements of sustained attention, but impairments of selective attention following the administration of ACTH-related neuropeptides. Under the influence of these peptides the attention is more easily attracted by stimuli, irrespective of their relevance.

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“…Of these four regions, the median eminence is the only brain region in which specific binding sites for blood-borne adrenocorticotropin have been demonstrated (1). In view of the various purportedly direct effects of blood-borne adrenocorticotropin and related peptides on brain function (3, 4), we have attempted to determine the cellular location and binding specificity of adrenocorticotropin binding sites in the rat median eminence by using quantitative light-and electron-microscope radioautography. In addition, we report the results of pilot radioautographic investigations of brain uptake of circulating adrenocorticotropin (5)(6)(7)(8).…”

mentioning

confidence: 99%

NH2-terminal specificity and axonal localization of adrenocorticotropin binding sites in rat median eminence.

Houten¹,

Khan²,

Walsh³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Adrenocorticotropin binding sites in the rat median eminence have been localized in vivo. These binding sites occur in the basalar zone, which is rich in axonal endings. Using competitive binding and quantitative light-microscope radioautography, we found that the median-eminence binding site, in contradistinction to the adrenal receptor, binds specifically the residue 4-10 region of the adrenocorticotropin molecule. Using quantitative electron-microscope radioautography and median-eminence deafferentation, we localized the binding sites to axon terminals in this region. In time-delayed uptake studies using light-microscope radioautography, we failed to observe concentration of radiolabel in neurons of the medial basal hypothalamus after the direct injection of radioiodinated adrenocorticotropin(1-24) into the median eminence.Binding sites for blood-borne adrenocorticotropin (ACTH) have been localized to the rat median eminence by quantitative radioautography (1). The median eminence is one of the four circumventricular organs of the brain, which are targets for direct interaction with a variety of circulating peptide hormones (2). Of these four regions, the median eminence is the only brain region in which specific binding sites for blood-borne adrenocorticotropin have been demonstrated (1). In view of the various purportedly direct effects of blood-borne adrenocorticotropin and related peptides on brain function (3, 4), we have attempted to determine the cellular location and binding specificity of adrenocorticotropin binding sites in the rat median eminence by using quantitative light-and electron-microscope radioautography. In addition, we report the results of pilot radioautographic investigations of brain uptake of circulating adrenocorticotropin (5-8). METHODSSynthetic ACTH1-24 (Cortrosyn), a gift from Organon, was iodinated using lactoperoxidase under mild conditions for 30 sec, as described by McIlhinney and Schulster (8). Monoiodinated hormone prepared by this method has been shown to retain its steroidogenic properties and capacity to bind receptors isolated from rat adrenocortical cells (8). lodinated peptide was purified by the silicic acid adsorption method of Rees et al. (9) with minor modifications, as follows. Ten milligrams of silicic acid (Bio-Sil A, mesh 200-325, Bio-Rad), which had been suspended in 2 ml of 50 mM sodium phosphate buffer, pH 7.4, containing 1.5% (wt/vol) bovine serum albumin, was added to the iodination mixture to terminate the iodination reaction. After 30 min at room temperature, the pellet was washed three times with 2 ml of cold distilled water and once with 1 M HCl. The adsorbed hormone was eluted in 2 ml of acetone/water/acetic acid (40:59:1, vol/vol) and concentrated by evaporation under a stream of N2. The purified 125I-labeled ACTH1-24 (125I-ACTH1-24) had a specific activity of 124 ,uCi/,g (1 Ci = 37 GBq). After purification, >98% of the radioactivity could be adsorbed by silicic acid and >95% could be precipitated by 10% (wt/vol) trichloroacetic acid. The l...

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Structure-activity relationships of peptides derived from ACTH, β-LPH and MSH with regard to avoidance behavior in rats

Cited by 39 publications

References 175 publications

Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

ACTH and Attention in Humans:A Review

NH2-terminal specificity and axonal localization of adrenocorticotropin binding sites in rat median eminence.

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